Page last updated: 2024-12-07

mor-14

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Description

N-methyldeoxynojirimycin: glucosidase inhibitor [Medical Subject Headings (MeSH), National Library of Medicine, extracted Dec-2023]

Cross-References

ID SourceID
PubMed CID92381
CHEMBL ID75971
SCHEMBL ID2435206
MeSH IDM0103675

Synonyms (24)

Synonym
mor 14
n-methyldeoxynojirimycin
n-methylmoranoline3,4,5-piperidinetriol, 2-(hydroxymethyl)-1-methyl-, [2r-(2a,3b,4a,5b)]-
3,4,5-piperidinetriol, 2-(hydroxymethyl)-1-methyl-, [2r-(2a,3b,4a,5b)]-
3,4,5-piperidinetriol, 2-(hydroxymethyl)-1-methyl-, (2r,3r,4r,5s)-
(2r,3r,4r,5s)-2-(hydroxymethyl)-1-methyl-piperidine-3,4,5-triol
69567-10-8
n-methylmoranoline
n-methyl-1-deoxynojirimycin, >=98%
d-glucitol, 1,5-dideoxy-1,5-(methylimino)-
mor-14
(2r,3r,4r,5s)-2-(hydroxymethyl)-1-methylpiperidine-3,4,5-triol
bdbm18353
chembl75971 ,
AKOS006237428
unii-yzs8607g9z
yzs8607g9z ,
mor14
n-methyl moranoline
SCHEMBL2435206
W-203549
HY-U00090
DTXSID30875703
Q27294813
[information is derived through text-mining from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Roles (4)

RoleDescription
EC 3.2.1.20 (alpha-glucosidase) inhibitorAn EC 3.2.1.* (glycosidase) inhibitor that interferes with the action of alpha-glucosidase (EC 3.2.1.20).
anti-HIV agentAn antiviral agent that destroys or inhibits the replication of the human immunodeficiency virus.
plant metaboliteAny eukaryotic metabolite produced during a metabolic reaction in plants, the kingdom that include flowering plants, conifers and other gymnosperms.
cardioprotective agentAny protective agent that is able to prevent damage to the heart.
[role information is derived from Chemical Entities of Biological Interest (ChEBI), Hastings J, Owen G, Dekker A, Ennis M, Kale N, Muthukrishnan V, Turner S, Swainston N, Mendes P, Steinbeck C. (2016). ChEBI in 2016: Improved services and an expanding collection of metabolites. Nucleic Acids Res]

Drug Classes (3)

ClassDescription
tertiary amino compoundA compound formally derived from ammonia by replacing three hydrogen atoms by organyl groups.
hydroxypiperidine
piperidine alkaloid
[compound class information is derived from Chemical Entities of Biological Interest (ChEBI), Hastings J, Owen G, Dekker A, Ennis M, Kale N, Muthukrishnan V, Turner S, Swainston N, Mendes P, Steinbeck C. (2016). ChEBI in 2016: Improved services and an expanding collection of metabolites. Nucleic Acids Res]

Protein Targets (8)

Inhibition Measurements

ProteinTaxonomyMeasurementAverageMin (ref.)Avg (ref.)Max (ref.)Bioassay(s)
Maltase-glucoamylase, intestinalHomo sapiens (human)IC50 (µMol)0.12000.04003.46529.0000AID104668
Lysosomal acid glucosylceramidaseHomo sapiens (human)IC50 (µMol)75.50000.03002.35898.8000AID1797728
Lysosomal alpha-glucosidaseHomo sapiens (human)Ki0.05900.05901.75307.3000AID1819245
Sucrase-isomaltase, intestinalRattus norvegicus (Norway rat)IC50 (µMol)2.22000.04001.848310.0000AID208985; AID91639
Protein-lysine 6-oxidaseHomo sapiens (human)IC50 (µMol)75.50000.01001.19705.0000AID1797728
Lactase-phlorizin hydrolase Rattus norvegicus (Norway rat)IC50 (µMol)4.40000.12002.98674.4000AID99232
[prepared from compound, protein, and bioassay information from National Library of Medicine (NLM), extracted Dec-2023]

Biological Processes (99)

Processvia Protein(s)Taxonomy
maltose catabolic processMaltase-glucoamylase, intestinalHomo sapiens (human)
starch catabolic processMaltase-glucoamylase, intestinalHomo sapiens (human)
dextrin catabolic processMaltase-glucoamylase, intestinalHomo sapiens (human)
mitochondrion organizationLysosomal acid glucosylceramidaseHomo sapiens (human)
neuron projection developmentLysosomal acid glucosylceramidaseHomo sapiens (human)
glucosylceramide catabolic processLysosomal acid glucosylceramidaseHomo sapiens (human)
autophagyLysosomal acid glucosylceramidaseHomo sapiens (human)
lysosome organizationLysosomal acid glucosylceramidaseHomo sapiens (human)
cholesterol metabolic processLysosomal acid glucosylceramidaseHomo sapiens (human)
determination of adult lifespanLysosomal acid glucosylceramidaseHomo sapiens (human)
cellular response to starvationLysosomal acid glucosylceramidaseHomo sapiens (human)
response to pHLysosomal acid glucosylceramidaseHomo sapiens (human)
microglia differentiationLysosomal acid glucosylceramidaseHomo sapiens (human)
regulation of macroautophagyLysosomal acid glucosylceramidaseHomo sapiens (human)
antigen processing and presentationLysosomal acid glucosylceramidaseHomo sapiens (human)
lipid storageLysosomal acid glucosylceramidaseHomo sapiens (human)
cerebellar Purkinje cell layer formationLysosomal acid glucosylceramidaseHomo sapiens (human)
pyramidal neuron differentiationLysosomal acid glucosylceramidaseHomo sapiens (human)
respiratory electron transport chainLysosomal acid glucosylceramidaseHomo sapiens (human)
termination of signal transductionLysosomal acid glucosylceramidaseHomo sapiens (human)
lipid glycosylationLysosomal acid glucosylceramidaseHomo sapiens (human)
negative regulation of protein-containing complex assemblyLysosomal acid glucosylceramidaseHomo sapiens (human)
regulation of TOR signalingLysosomal acid glucosylceramidaseHomo sapiens (human)
positive regulation of proteasomal ubiquitin-dependent protein catabolic processLysosomal acid glucosylceramidaseHomo sapiens (human)
negative regulation of interleukin-6 productionLysosomal acid glucosylceramidaseHomo sapiens (human)
T cell differentiation in thymusLysosomal acid glucosylceramidaseHomo sapiens (human)
response to testosteroneLysosomal acid glucosylceramidaseHomo sapiens (human)
positive regulation of protein dephosphorylationLysosomal acid glucosylceramidaseHomo sapiens (human)
proteasome-mediated ubiquitin-dependent protein catabolic processLysosomal acid glucosylceramidaseHomo sapiens (human)
positive regulation of protein-containing complex disassemblyLysosomal acid glucosylceramidaseHomo sapiens (human)
negative regulation of MAP kinase activityLysosomal acid glucosylceramidaseHomo sapiens (human)
negative regulation of neuron apoptotic processLysosomal acid glucosylceramidaseHomo sapiens (human)
response to estrogenLysosomal acid glucosylceramidaseHomo sapiens (human)
sphingosine biosynthetic processLysosomal acid glucosylceramidaseHomo sapiens (human)
ceramide biosynthetic processLysosomal acid glucosylceramidaseHomo sapiens (human)
cell maturationLysosomal acid glucosylceramidaseHomo sapiens (human)
brain morphogenesisLysosomal acid glucosylceramidaseHomo sapiens (human)
homeostasis of number of cellsLysosomal acid glucosylceramidaseHomo sapiens (human)
negative regulation of inflammatory responseLysosomal acid glucosylceramidaseHomo sapiens (human)
neuromuscular processLysosomal acid glucosylceramidaseHomo sapiens (human)
neuron apoptotic processLysosomal acid glucosylceramidaseHomo sapiens (human)
establishment of skin barrierLysosomal acid glucosylceramidaseHomo sapiens (human)
microglial cell proliferationLysosomal acid glucosylceramidaseHomo sapiens (human)
motor behaviorLysosomal acid glucosylceramidaseHomo sapiens (human)
cellular response to tumor necrosis factorLysosomal acid glucosylceramidaseHomo sapiens (human)
hematopoietic stem cell proliferationLysosomal acid glucosylceramidaseHomo sapiens (human)
response to dexamethasoneLysosomal acid glucosylceramidaseHomo sapiens (human)
lymphocyte migrationLysosomal acid glucosylceramidaseHomo sapiens (human)
response to thyroid hormoneLysosomal acid glucosylceramidaseHomo sapiens (human)
beta-glucoside catabolic processLysosomal acid glucosylceramidaseHomo sapiens (human)
positive regulation of protein lipidationLysosomal acid glucosylceramidaseHomo sapiens (human)
positive regulation of neuronal action potentialLysosomal acid glucosylceramidaseHomo sapiens (human)
positive regulation of autophagy of mitochondrion in response to mitochondrial depolarizationLysosomal acid glucosylceramidaseHomo sapiens (human)
autophagosome organizationLysosomal acid glucosylceramidaseHomo sapiens (human)
regulation of lysosomal protein catabolic processLysosomal acid glucosylceramidaseHomo sapiens (human)
maltose metabolic processLysosomal alpha-glucosidaseHomo sapiens (human)
regulation of the force of heart contractionLysosomal alpha-glucosidaseHomo sapiens (human)
diaphragm contractionLysosomal alpha-glucosidaseHomo sapiens (human)
heart morphogenesisLysosomal alpha-glucosidaseHomo sapiens (human)
glycogen catabolic processLysosomal alpha-glucosidaseHomo sapiens (human)
sucrose metabolic processLysosomal alpha-glucosidaseHomo sapiens (human)
glucose metabolic processLysosomal alpha-glucosidaseHomo sapiens (human)
lysosome organizationLysosomal alpha-glucosidaseHomo sapiens (human)
locomotory behaviorLysosomal alpha-glucosidaseHomo sapiens (human)
tissue developmentLysosomal alpha-glucosidaseHomo sapiens (human)
aorta developmentLysosomal alpha-glucosidaseHomo sapiens (human)
vacuolar sequesteringLysosomal alpha-glucosidaseHomo sapiens (human)
muscle cell cellular homeostasisLysosomal alpha-glucosidaseHomo sapiens (human)
neuromuscular process controlling postureLysosomal alpha-glucosidaseHomo sapiens (human)
neuromuscular process controlling balanceLysosomal alpha-glucosidaseHomo sapiens (human)
cardiac muscle contractionLysosomal alpha-glucosidaseHomo sapiens (human)
glycophagyLysosomal alpha-glucosidaseHomo sapiens (human)
osteoblast differentiationProtein-lysine 6-oxidaseHomo sapiens (human)
regulation of protein phosphorylationProtein-lysine 6-oxidaseHomo sapiens (human)
heart developmentProtein-lysine 6-oxidaseHomo sapiens (human)
response to xenobiotic stimulusProtein-lysine 6-oxidaseHomo sapiens (human)
regulation of gene expressionProtein-lysine 6-oxidaseHomo sapiens (human)
regulation of striated muscle tissue developmentProtein-lysine 6-oxidaseHomo sapiens (human)
regulation of transforming growth factor beta receptor signaling pathwayProtein-lysine 6-oxidaseHomo sapiens (human)
peptidyl-lysine oxidationProtein-lysine 6-oxidaseHomo sapiens (human)
bone mineralizationProtein-lysine 6-oxidaseHomo sapiens (human)
lung developmentProtein-lysine 6-oxidaseHomo sapiens (human)
platelet-derived growth factor receptor-beta signaling pathwayProtein-lysine 6-oxidaseHomo sapiens (human)
ascending aorta developmentProtein-lysine 6-oxidaseHomo sapiens (human)
descending aorta developmentProtein-lysine 6-oxidaseHomo sapiens (human)
protein modification processProtein-lysine 6-oxidaseHomo sapiens (human)
regulation of apoptotic processProtein-lysine 6-oxidaseHomo sapiens (human)
regulation of megakaryocyte differentiationProtein-lysine 6-oxidaseHomo sapiens (human)
muscle cell cellular homeostasisProtein-lysine 6-oxidaseHomo sapiens (human)
elastic fiber assemblyProtein-lysine 6-oxidaseHomo sapiens (human)
blood vessel morphogenesisProtein-lysine 6-oxidaseHomo sapiens (human)
response to steroid hormoneProtein-lysine 6-oxidaseHomo sapiens (human)
negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transductionProtein-lysine 6-oxidaseHomo sapiens (human)
muscle cell developmentProtein-lysine 6-oxidaseHomo sapiens (human)
cell chemotaxisProtein-lysine 6-oxidaseHomo sapiens (human)
connective tissue developmentProtein-lysine 6-oxidaseHomo sapiens (human)
DNA biosynthetic processProtein-lysine 6-oxidaseHomo sapiens (human)
regulation of bone developmentProtein-lysine 6-oxidaseHomo sapiens (human)
cellular response to chemokineProtein-lysine 6-oxidaseHomo sapiens (human)
regulation of platelet-derived growth factor receptor-beta signaling pathwayProtein-lysine 6-oxidaseHomo sapiens (human)
collagen fibril organizationProtein-lysine 6-oxidaseHomo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Molecular Functions (19)

Processvia Protein(s)Taxonomy
catalytic activityMaltase-glucoamylase, intestinalHomo sapiens (human)
glucan 1,4-alpha-glucosidase activityMaltase-glucoamylase, intestinalHomo sapiens (human)
alpha-1,4-glucosidase activityMaltase-glucoamylase, intestinalHomo sapiens (human)
protein bindingMaltase-glucoamylase, intestinalHomo sapiens (human)
amylase activityMaltase-glucoamylase, intestinalHomo sapiens (human)
carbohydrate bindingMaltase-glucoamylase, intestinalHomo sapiens (human)
maltose alpha-glucosidase activityMaltase-glucoamylase, intestinalHomo sapiens (human)
galactosylceramidase activityLysosomal acid glucosylceramidaseHomo sapiens (human)
glucosylceramidase activityLysosomal acid glucosylceramidaseHomo sapiens (human)
signaling receptor bindingLysosomal acid glucosylceramidaseHomo sapiens (human)
scavenger receptor bindingLysosomal acid glucosylceramidaseHomo sapiens (human)
protein bindingLysosomal acid glucosylceramidaseHomo sapiens (human)
glucosyltransferase activityLysosomal acid glucosylceramidaseHomo sapiens (human)
steryl-beta-glucosidase activityLysosomal acid glucosylceramidaseHomo sapiens (human)
alpha-1,4-glucosidase activityLysosomal alpha-glucosidaseHomo sapiens (human)
carbohydrate bindingLysosomal alpha-glucosidaseHomo sapiens (human)
maltose alpha-glucosidase activityLysosomal alpha-glucosidaseHomo sapiens (human)
alpha-glucosidase activityLysosomal alpha-glucosidaseHomo sapiens (human)
protein-lysine 6-oxidase activityProtein-lysine 6-oxidaseHomo sapiens (human)
copper ion bindingProtein-lysine 6-oxidaseHomo sapiens (human)
protein bindingProtein-lysine 6-oxidaseHomo sapiens (human)
collagen bindingProtein-lysine 6-oxidaseHomo sapiens (human)
small molecule bindingProtein-lysine 6-oxidaseHomo sapiens (human)
molecular adaptor activityProtein-lysine 6-oxidaseHomo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Ceullar Components (19)

Processvia Protein(s)Taxonomy
plasma membraneMaltase-glucoamylase, intestinalHomo sapiens (human)
apical plasma membraneMaltase-glucoamylase, intestinalHomo sapiens (human)
extracellular exosomeMaltase-glucoamylase, intestinalHomo sapiens (human)
tertiary granule membraneMaltase-glucoamylase, intestinalHomo sapiens (human)
ficolin-1-rich granule membraneMaltase-glucoamylase, intestinalHomo sapiens (human)
lysosomeLysosomal acid glucosylceramidaseHomo sapiens (human)
lysosomal membraneLysosomal acid glucosylceramidaseHomo sapiens (human)
endoplasmic reticulumLysosomal acid glucosylceramidaseHomo sapiens (human)
Golgi apparatusLysosomal acid glucosylceramidaseHomo sapiens (human)
trans-Golgi networkLysosomal acid glucosylceramidaseHomo sapiens (human)
lysosomal lumenLysosomal acid glucosylceramidaseHomo sapiens (human)
extracellular exosomeLysosomal acid glucosylceramidaseHomo sapiens (human)
lysosomeLysosomal alpha-glucosidaseHomo sapiens (human)
lysosomal membraneLysosomal alpha-glucosidaseHomo sapiens (human)
plasma membraneLysosomal alpha-glucosidaseHomo sapiens (human)
membraneLysosomal alpha-glucosidaseHomo sapiens (human)
azurophil granule membraneLysosomal alpha-glucosidaseHomo sapiens (human)
lysosomal lumenLysosomal alpha-glucosidaseHomo sapiens (human)
intracellular membrane-bounded organelleLysosomal alpha-glucosidaseHomo sapiens (human)
extracellular exosomeLysosomal alpha-glucosidaseHomo sapiens (human)
tertiary granule membraneLysosomal alpha-glucosidaseHomo sapiens (human)
ficolin-1-rich granule membraneLysosomal alpha-glucosidaseHomo sapiens (human)
autolysosome lumenLysosomal alpha-glucosidaseHomo sapiens (human)
extracellular regionProtein-lysine 6-oxidaseHomo sapiens (human)
extracellular spaceProtein-lysine 6-oxidaseHomo sapiens (human)
collagen trimerProtein-lysine 6-oxidaseHomo sapiens (human)
extracellular spaceProtein-lysine 6-oxidaseHomo sapiens (human)
collagen-containing extracellular matrixProtein-lysine 6-oxidaseHomo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Bioassays (20)

Assay IDTitleYearJournalArticle
AID104771Concentration giving 50% inhibition of growth of mock-infected MT-4 cells1995Journal of medicinal chemistry, Jun-23, Volume: 38, Issue:13
N-alkylated nitrogen-in-the-ring sugars: conformational basis of inhibition of glycosidases and HIV-1 replication.
AID35369Inhibition of lysosomal Alpha-mannosidase II in rat liver1995Journal of medicinal chemistry, Jun-23, Volume: 38, Issue:13
N-alkylated nitrogen-in-the-ring sugars: conformational basis of inhibition of glycosidases and HIV-1 replication.
AID36809Inhibition of lysosomal Alpha-Glucosidase II in rat liver1995Journal of medicinal chemistry, Jun-23, Volume: 38, Issue:13
N-alkylated nitrogen-in-the-ring sugars: conformational basis of inhibition of glycosidases and HIV-1 replication.
AID105142Concentration giving 50% inhibition of HIV-1 induced cytopathogenicity in MT-4 cells1995Journal of medicinal chemistry, Jun-23, Volume: 38, Issue:13
N-alkylated nitrogen-in-the-ring sugars: conformational basis of inhibition of glycosidases and HIV-1 replication.
AID35262Inhibition of golgi Alpha-mannosidase II in rat liver1995Journal of medicinal chemistry, Jun-23, Volume: 38, Issue:13
N-alkylated nitrogen-in-the-ring sugars: conformational basis of inhibition of glycosidases and HIV-1 replication.
AID35368Competitive Inhibitory activity against Golgi Alpha-mannosidase II1995Journal of medicinal chemistry, Jun-23, Volume: 38, Issue:13
N-alkylated nitrogen-in-the-ring sugars: conformational basis of inhibition of glycosidases and HIV-1 replication.
AID208985Inhibition of Sucrase in rat intestinal brush border membranes by D-glucose oxidase-peroxidase method1995Journal of medicinal chemistry, Jun-23, Volume: 38, Issue:13
N-alkylated nitrogen-in-the-ring sugars: conformational basis of inhibition of glycosidases and HIV-1 replication.
AID210969Inhibition of Glycosidases (trehalase)in rat intestinal brush border membranes by D-glucose oxidase-peroxidase method1995Journal of medicinal chemistry, Jun-23, Volume: 38, Issue:13
N-alkylated nitrogen-in-the-ring sugars: conformational basis of inhibition of glycosidases and HIV-1 replication.
AID35370Inhibition of soluble Alpha-mannosidase II in rat liver1995Journal of medicinal chemistry, Jun-23, Volume: 38, Issue:13
N-alkylated nitrogen-in-the-ring sugars: conformational basis of inhibition of glycosidases and HIV-1 replication.
AID104668Inhibition of Glycosidases (maltase) in rat intestinal brush border membranes by D-glucose oxidase-peroxidase method maltase1995Journal of medicinal chemistry, Jun-23, Volume: 38, Issue:13
N-alkylated nitrogen-in-the-ring sugars: conformational basis of inhibition of glycosidases and HIV-1 replication.
AID36808Inhibition of endoplasmic reticulum Alpha-Glucosidase II in rat liver1995Journal of medicinal chemistry, Jun-23, Volume: 38, Issue:13
N-alkylated nitrogen-in-the-ring sugars: conformational basis of inhibition of glycosidases and HIV-1 replication.
AID1819245Inhibition of human GAA using 4-methylumbelliferyl-alpha-D-glucopyranoside as substrate preincubated for 45 min followed by substrate addition and measured after 30 min by fluorescence spectrophotometer analysis2022Journal of medicinal chemistry, 02-10, Volume: 65, Issue:3
5-
AID36810Competitive Inhibitory activity against Endoplasmic reticulum Alpha-Glucosidase II1995Journal of medicinal chemistry, Jun-23, Volume: 38, Issue:13
N-alkylated nitrogen-in-the-ring sugars: conformational basis of inhibition of glycosidases and HIV-1 replication.
AID105269Concentration giving 50% inhibition of HIV-1 induced cytopathogenicity in MOLT-4 cells1995Journal of medicinal chemistry, Jun-23, Volume: 38, Issue:13
N-alkylated nitrogen-in-the-ring sugars: conformational basis of inhibition of glycosidases and HIV-1 replication.
AID105266Concentration giving 50% inhibition of growth of mock-infected MOLT-4 cells1995Journal of medicinal chemistry, Jun-23, Volume: 38, Issue:13
N-alkylated nitrogen-in-the-ring sugars: conformational basis of inhibition of glycosidases and HIV-1 replication.
AID521220Inhibition of neurosphere proliferation of mouse neural precursor cells by MTT assay2007Nature chemical biology, May, Volume: 3, Issue:5
Chemical genetics reveals a complex functional ground state of neural stem cells.
AID91639Inhibition of Glycosidases (isomaltase)in rat intestinal brush border membranes by D-glucose oxidase-peroxidase method1995Journal of medicinal chemistry, Jun-23, Volume: 38, Issue:13
N-alkylated nitrogen-in-the-ring sugars: conformational basis of inhibition of glycosidases and HIV-1 replication.
AID99232Inhibition of Glycosidases (lactase)in rat intestinal brush border membranes by D-glucose oxidase-peroxidase method1995Journal of medicinal chemistry, Jun-23, Volume: 38, Issue:13
N-alkylated nitrogen-in-the-ring sugars: conformational basis of inhibition of glycosidases and HIV-1 replication.
AID52058Inhibition of Cellobiase in rat intestinal brush border membranes by D-glucose oxidase-peroxidase method1995Journal of medicinal chemistry, Jun-23, Volume: 38, Issue:13
N-alkylated nitrogen-in-the-ring sugars: conformational basis of inhibition of glycosidases and HIV-1 replication.
AID1797728In Vitro Enzyme Inhibition from Article 10.1016/j.bmc.2006.08.003: \\Alpha-1-C-octyl-1-deoxynojirimycin as a pharmacological chaperone for Gaucher disease.\\2006Bioorganic & medicinal chemistry, Dec-01, Volume: 14, Issue:23
Alpha-1-C-octyl-1-deoxynojirimycin as a pharmacological chaperone for Gaucher disease.
[information is prepared from bioassay data collected from National Library of Medicine (NLM), extracted Dec-2023]

Research

Studies (47)

TimeframeStudies, This Drug (%)All Drugs %
pre-199022 (46.81)18.7374
1990's18 (38.30)18.2507
2000's6 (12.77)29.6817
2010's0 (0.00)24.3611
2020's1 (2.13)2.80
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Market Indicators

Research Demand Index: 20.07

According to the monthly volume, diversity, and competition of internet searches for this compound, as well the volume and growth of publications, there is estimated to be moderate demand-to-supply ratio for research on this compound.

MetricThis Compound (vs All)
Research Demand Index20.07 (24.57)
Research Supply Index3.87 (2.92)
Research Growth Index4.16 (4.65)
Search Engine Demand Index29.35 (26.88)
Search Engine Supply Index3.00 (0.95)

This Compound (20.07)

All Compounds (24.57)

Study Types

Publication TypeThis drug (%)All Drugs (%)
Trials0 (0.00%)5.53%
Reviews1 (2.13%)6.00%
Case Studies0 (0.00%)4.05%
Observational0 (0.00%)0.25%
Other46 (97.87%)84.16%
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]